ID D8PMP5_SCHCM Unreviewed; 1450 AA.
AC D8PMP5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Lysophospholipase NTE1 {ECO:0000256|ARBA:ARBA00018317, ECO:0000256|RuleBase:RU362043};
DE EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362043};
DE AltName: Full=Intracellular phospholipase B {ECO:0000256|RuleBase:RU362043};
GN ORFNames=SCHCODRAFT_72754 {ECO:0000313|EMBL:EFJ02164.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFJ02164.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
CC -!- FUNCTION: Intracellular phospholipase B that catalyzes the double
CC deacylation of phosphatidylcholine (PC) to glycerophosphocholine
CC (GroPCho). Plays an important role in membrane lipid homeostasis.
CC {ECO:0000256|RuleBase:RU362043}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000256|RuleBase:RU362043};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU362043}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636,
CC ECO:0000256|RuleBase:RU362043}.
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DR EMBL; GL377302; EFJ02164.1; -; Genomic_DNA.
DR RefSeq; XP_003037066.1; XM_003037020.1.
DR STRING; 578458.D8PMP5; -.
DR GeneID; 9597510; -.
DR KEGG; scm:SCHCO_02530966; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02530966; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_1_1; -.
DR InParanoid; D8PMP5; -.
DR OMA; SSGYVWR; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000007431; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR001423; LysoPLipase_patatin_CS.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 2.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS01237; UPF0028; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU362043};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW ProRule:PRU01161}; Membrane {ECO:0000256|RuleBase:RU362043};
KW Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW Transmembrane {ECO:0000256|RuleBase:RU362043};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362043}.
FT TRANSMEM 27..57
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT DOMAIN 652..760
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 773..893
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1144..1308
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 278..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1148..1153
FT /note="GXGXXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT MOTIF 1175..1179
FT /note="GXSXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT MOTIF 1295..1297
FT /note="DGA/G"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT COMPBIAS 283..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1177
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1295
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 1450 AA; 159537 MW; 6E07A9BAE99CDF9E CRC64;
MSELSPDVSA SATAAAADVS SHPLVSLISA CFWVILWALS WVKSLIGIVT ISVPRLVYQI
LSYSMTLTLN FWSFVLIFGT CAVALNYFIR FRYLNDYMQL KEPPLGKPDV KELHPDVNTA
DEPANFHNYL DDFLQAVRVF GFLEKPVFHE LARHLQTRRL IAGDSISLDQ DRSFYCVVDG
TVQVFAKSDD EHTASGSGQW DDEDINGYHL MNEVTSGGTV SSLFTILSLF TEDVKISWQD
ADESPKRTHR SRKSTDERIR VNSDVSYFNL ERPALVRTPL SNPGLRRRSS TSSSASTVQP
EESPTTPEDL RRTASPPPLS ERSYAPSTPV HHIQGPVQIH RGVVARATED TTLAVIPAEA
FRRLTKKFPK ATGHIVQVIL TRFARVTFNA AHKYLGLTSE VLRAEKSIND LACHPLPPSF
YEGGGLQQLR HRFEVPPSGS DSDNDYFTHT GARTHSPNPM STYSPNPMSA QESSTDSDDS
HPAFIRTASS STARPGSRSS TISSPNLTKT SGSRMNVQAG DLLSSTANTS RLLRPINRTA
MTPRVPLRAV VEHQSPERAL GEEFNLREEV MSCIAKSIGL LQPPISGNDS LEGSPKLNPF
ERSRSPMPSS FGSLSLLDLG DDASSTMTGG SASIQSGSGM SGLDNEVEIL FFPAGATLTK
AGDISTGLYY VIEGFLDILL PLEKEKQRAS DRPGAKNPGK GPNKKPHDDS ETHKFLFTVK
PGGIAGYLAS LSNTASYVDI VAKTDTYVGY LPAQALERLL EKRPIVLLTL AKRLISLLSP
LVLQIDASLD WMQVNAGQII WRPEDASDCF YIVINGRLRA ITETEKGDVS IVGEYGQGDA
VGELDVITSS PRQNTLHAIR DTELIRMPQT LFNALSMRDP RTTQQILRKI ALRVRDEAEG
GKTSQSRPPM EVKSSNANLK TICILPVSRA VPIDVFARKL QTALEGIGAS TVYLNQASVA
NRLGRHVFTR MGKLKAAGWL ADQEQRYRTV LYVADSPVNN SWTQTCIRQA DCVMVVGMGD
DASIGEYERL LLSTKTTAKK ELVLLHPDRS VAPGSTREWL KNRPWIHQHI HVELPGLVIP
ITKSTAHLPK DPDPIIALKN FKDKVQSELK KYRGTVGDAR PQRLPHVNDF SRLARRICGK
SIGLVLGGGG ARGVSHLGLI RALEEYGIPV DHVGGTSIGA FIGGLYAREG DSLSSAGRAK
QFSGRMGNIW RMLSDVTYPI VAYTTGHEFN RAIYKSFYDL HIEDMWLPFF CNTTNITTSG
MDIHETGYAW RFIRGSMTLV GLLPPLCDNG NMHVDGGYVD NLPVSTMFSM GSSAVFACDV
GSIDDNSPRN FGDSVSGWWL FINRWNPFSD ASRVPAITEI QSRLAYVSSV RTLEEAKVAP
GCLYIAMPVQ EYGTLQFSKF EELQKIGYEA GMKALAKWDE EGRLPSPFID GKQQFSSSKK
QGRAARRNSI
//